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Originally published In Press as doi:10.1074/jbc.M109984200 on December 26, 2001

J. Biol. Chem., Vol. 277, Issue 10, 8243-8247, March 8, 2002
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A Novel WD Repeat Protein Component of the Methylosome Binds Sm Proteins*

Westley J. FriesenDagger , Anastasia WyceDagger , Sergey PaushkinDagger , Linda AbelDagger , Juri Rappsilber§, Matthias Mann§||, and Gideon DreyfussDagger **

From the Dagger  Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6148 and the § Protein Interaction Laboratory, Center for Experimental Bioinformatics and Department of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense M, Denmark

We have recently described a large (20 S) protein arginine methyltransferase complex, termed the methylosome, that contains the methyltransferase JBP1 (PRMT5) and the pICln protein. The methylosome functions to modify specific arginines to dimethylarginines in the arginine- and glycine-rich domains of several spliceosomal Sm proteins, and this modification targets these proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein (snRNP) core particles. Here, we describe a novel component of the methylosome, a 50-kilodalton WD repeat protein termed methylosome protein 50 (MEP50). We show that MEP50 is important for methylosome activity and binds to JBP1 and to a subset of Sm proteins. Because WD repeat proteins provide a platform for multiple protein interactions, MEP50 may function to mediate the interaction of multiple substrates with the methylosome. Interestingly, all of the known components of the methylosome bind Sm proteins, suggesting that in addition to producing properly methylated substrates for the SMN complex, the methylosome may be involved in Sm protein rearrangements or pre-assembly required for snRNP biogenesis.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF478464 (MEP50).

A Marie Curie fellow.

|| Supported by a fund of the Danish National Research Foundation to the Center of Experimental Bioinformatics.

** An Investigator of the Howard Hughes Medical Institute; supported by the Association Française contre les Myopathies and by a grant from the National Institutes of Health. To whom correspondence should be addressed. Tel.: 215-898-0398, Fax: 215-573-2000, E-mail: gdreyfuss@hhmi.upenn.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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